Research workbench
The structure of binary complex between a mammalian mevalonate kinase and ATP: insights into the reaction mechanism and human inherited disease
Analyse The structure of binary complex between a mammalian mevalonate kinase and ATP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KVK
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mevalonate kinase
- EC
- 2.7.1.36
- UniProt
- P17256
- Ligands
- ATP, MG
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mevalonate kinase (EC 2.7.1.36) | protein | 378 | 45% helix, 22% strand | P17256 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 529 | 0.69 | 0.79 | 49 | MG, ATP |
| 2 | 81 | 0.42 | 0.79 | 17 | empty |
| 3 | 95 | 0.40 | 0.77 | 18 | empty |
Compared structures
- 1KVK · The Structure of Binary complex between a Mammalian Mevalonate Kinase and ATP: Insights… · the same entry in another collection · chain A against A, TM-score 1.00
- P17256 · AlphaFold monomer V2.0 prediction for mevalonate kinase (P17256) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P17256
- Elsewhere: RCSB PDB 1KVK · PDBe 1KVK · UniProt P17256
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